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ProteomicsSerine ADP-ribosylation in Drosophila provides insights into the evolution of reversible ADP-ribosylation signaling
In the mammalian DNA damage response, ADP-ribosylation signaling is of crucial importance to mark sites of DNA damage as well as recruit and regulate repairs factors. Specifically, the PARP1:HPF1 complex recognizes damaged DNA and catalyzes the formation of serine-linked ADP-ribosylation marks (mono...
ORGANISM(S): Drosophila melanogaster (Fruit fly) 
2023-05-26 | PXD036512 | Pride
Proteomics Adpr Ethcd Parp Drosophila Parg Af1521 Adp-ribosylation 
ProteomicsAn advanced strategy for comprehensive profiling of ADP-ribosylation sites using mass spectrometry-based proteomics
ADP-ribosylation is a widespread post-translational modification (PTM) with crucial functions in many cellular processes. Here, we describe an in-depth ADP-ribosylome using our Af1521-based proteomics methodology for profiling of ADP-ribosylation sites, by systematically assessing complementary prot...
ORGANISM(S): Homo sapiens (Human) 
2019-02-26 | PXD012243 | Pride
Adpr Human Ethcd Parp Lumos Etd Lysc Trypsin Adp-ribosylation 
ProteomicsTemporal and site-specific ADP-ribosylation dynamics upon different genotoxic stresses
The DNA damage response revolves around transmission of information via post-translational modifications, including reversible protein ADP-ribosylation. Here, we applied a mass spectrometry-based Af1521 enrichment technology for the identification and quantification of ADP-ribosylation sites as a fu...
ORGANISM(S): Homo sapiens (Human) 
2021-11-04 | PXD028902 | Pride
Proteomics Mass spectrometry Parp Post-translational modification Dna damage Af1521 Adp-ribosylation 
UnknownReversal of tyrosine-linked ADP-ribosylation by ARH3 and PARG.
Not available
S-EPMC11541775 | biostudies-literature
ProteomicsMapping physiological ADP-ribosylation using Activated Ion Electron Transfer Dissociation (AI-ETD)
ADP-ribosylation (ADPr) is a post-translational modification that plays pivotal roles in a wide range of cellular processes. Mass spectrometry (MS)-based analysis of ADPr under physiological conditions, without relying on genetic or chemical perturbation, has been hindered by technical limitations. ...
ORGANISM(S): Homo sapiens (Human) 
2020-09-23 | PXD017417 | Pride
Activated ion electron transfer dissociation Post-translational modification Adpr Ptm Parp Ai-etd Adp-ribosylation 
ProteomicsSystems-wide analysis of serine-ADP-ribosylation reveals widespread occurrence and site-specific overlap with phosphorylation (part 2, phosphorylation data)
Here we report systems-wide identification of serine ADP-ribosylation sites and quantification of their cellular changes in human cells upon oxidative stress. High-resolution mass spectrometry and unrestricted data processing confirmed that serine residues are the major target of ADP-ribosylation in...
ORGANISM(S): Homo sapiens (Human) 
2018-08-29 | PXD009931 | Pride
Phosphorylation Adp Adp-ribosylation 
ProteomicsThe regulatory landscape of the human HPF1- and ARH3-dependent ADP-ribosylome (part 1)
Despite the involvement of Poly(ADP-ribose) polymerase-1 (PARP1) in many important biological pathways, the target residues of PARP1-mediated ADP-ribosylation remain ambiguous. To explicate the ADP-ribosylation regulome, we analyze human cells depleted for key regulators of PARP1 activity, histone P...
ORGANISM(S): Homo sapiens (Human) 
2021-10-07 | PXD023835 | Pride
Parp1 Adpr Hpf1 Arh3 Par Parg Af1521 Mar Adp-ribosylation 
UnknownCis- and trans-resveratrol have opposite effects on histone serine-ADP-ribosylation and tyrosine induced neurodegeneration.
Not available
S-EPMC9187644 | biostudies-literature
ProteomicsA site-specific analysis of the ADP-Ribosylome unveils Homogeneous Serine ADP-Ribosylation across wild-type and BRCA-mutant Breast Cancer cell lines
ADP-ribosylation (ADPr) signaling plays a crucial role in the DNA damage response. Inhibitors against the main enzyme catalyzing ADPr after DNA damage – PARP1 – are used as targeted therapies against breast cancers with BRCA1/2 mutations. However, development of resistance to PARP inhibitors (PARPi)...
ORGANISM(S): Homo sapiens (Human) 
2024-08-02 | PXD047613 | Pride
Proteomics Mass spectrometry Ethcd Parp inhibitor sensitivity Parp Af1521 macrodomain Adp-ribosylome Parg Adp-ribosylation 
ProteomicsGas-phase Fragmentation of ADP-Ribosylated Peptides: Arginine-Specific Side-Chain Losses and their Implication in Database Searches
ADP-ribosylation is a reversible post-translational modification of proteins that has been linked to many biological processes. The identification of ADP-ribosylated proteins and of their acceptor amino acids remains a significant challenge. The attachment sites of the modification are difficult to ...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2021-05-19 | PXD017013 | Pride
Post-translational modification Arginine Mass spectrometry Marker ion Neutral loss Adp-ribosylation Orbitrap fusion 
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